Three-dimensional homology models for Trypanosoma cruzi ribosomal stalk p proteins

AMANTE ,ANALIA; GÓMEZ BARROZO JA; AGUILAR, CF

San Luis

Congreso; XXXV Reunión Científica Anual de la Sociedad de Biología de Cuyo; 2018

SBC

Trypanosoma cruzi is the etiologic agent of the Chagas´ disease. This work intends to study the three-dimensional structure of T. cruziribosomal complex stalk in the large subunit of the ribosomes. Ribosomal proteins are involved in important metabolic processes and inthe development of Chagas´ disease pathology. The stalk is formed by the P proteins: TcP0, TcP1a, TcP1β, TcP2a and TcP2β. TcP0protein has 34 kDa, TcP1 and TcP2 proteins are smaller with a molecular weight of 10 kDa. The crystallographic structure of T. cruzi P0and the stalk complex TcP0-TcP1α-TcP1β-TcP2α-TcP2β have not been solved to date. A homology model for TcP0 has been obtained inour laboratory. Additionally, we have made three dimensional homology molecular models for the four small P proteins using theModeller program. These proteins are formed by three structural domains: an N-terminal α?domain, an inherently unstructured coiled Arichdomain and a C-terminal negatively charged domain. TcP0 is formed by a N-terminal globular domain, an alpha domain, adisordered region and a C-terminal negative tail. Observations of both the molecular electrostatic potential and the hydrophobic surfacesfor the P proteins suggest a model for the formation of a pentameric complex. We have explored and identified protein interactions thatmay be involved in conformational stability. This work represents an important three dimensional characterization for these T. cruziproteins and provide clues for understand its functional properties.